Abstract Unpredictable variation in quality, including fresh pork water-holding capacity, remains challenging to pork processors and customers. Defining the diverse factors that influence fresh pork water-holding capacity is necessary to make progress in refining pork quality prediction methods. The objective was to utilize liquid chromatography and mass spectrometry coupled with tandem mass tag (TMT) multiplexing to evaluate the sarcoplasmic proteome of aged pork loins classified by purge loss. Fresh commercial pork loins were collected, aged 12 or 14 d postmortem, and pork quality and sensory attributes were evaluated. Chops were classified into Low (N = 27, average purge = 0.33%), Intermediate (N = 27, average purge = 0.72%), or High (N = 27, average purge = 1.19%) chop purge groups. Proteins soluble in a low-ionic strength buffer were extracted, digested with trypsin, labeled with 11-plex isobaric TMT reagents, and detected using a Q-Exactive Mass Spectrometer. Between the Low and High purge groups, 40 proteins were differentially (P < 0.05) abundant. The Low purge group had a greater abundance of proteins classified as structural and contractile, sarcoplasmic reticulum and calcium regulating, chaperone, and citric acid cycle enzymes than the High purge group. The presence of myofibrillar proteins in the aged sarcoplasmic proteome is likely due to postmortem degradation. These observations support our hypothesis that pork chops with low purge have a greater abundance of structural proteins in the soluble protein fraction. Together, these and other proteins in the aged sarcoplasmic proteome may be biomarkers of pork water-holding capacity. Additional research should establish the utility of these proteins as biomarkers early postmortem and over subsequent aging periods. The fractionation and proteomic analysis of the aged sarcoplasmic proteome offers an unparalleled view of the postmortem biochemical and proteolytic events associated with pork water-holding capacity. Lay Summary Fresh pork can vary in its ability to retain water—commonly termed as its water-holding capacity—where a greater water-holding capacity means it retains more water as it is cut, packaged, and stored. However, commercial pork loins have considerable variability in their water-holding capacity, which can impact the consumer’s eating experience. This study aimed to examine water-soluble proteins from aged commercial pork chops and to identify and quantify these proteins with mass spectrometry to confirm the previous observation that the degradation of specific structural proteins is associated with greater water-holding capacity. This analysis identified 40 proteins differentially abundant between pork chops with varying water-holding capacities. Pork chops with greater water-holding capacity had a greater abundance of proteins classified as structural and contractile, calcium regulating, and chaperone. Metabolic proteins were also differentially abundant in aged pork loins with differing water-holding capacity. This study confirmed previous observations that the degradation of key structural proteins is associated with greater water-holding capacity while identifying new proteins that may be biomarkers for water-holding capacity.